Conventional therapeutics can be broadly divided into two classes: small molecules and biologics. Small molecules typically have a mass of <1000 Da and bind with high affinity to hydrophobic pockets in proteins, and many are capable of penetrating cells. Biologics are biomolecules, usually proteins (such as antibodies or hormones) that can bind the surfaces of other biomolecules with high affinity and specificity, but are unable to efficiently enter cells. It has been estimated that only ˜12% of human proteins contain a hydrophobic pocket capable of binding small molecules with high affinity, and that less than 10% of human proteins are secreted (i.e., transported outside of the cell). As these two groups are not mutually exclusive, more than 78% of human proteins are therefore inside the cell but lack a hydrophobic binding pocket. These proteins, along with others that are intracellular and contain intractable hydrophobic pockets, are often referred to as “undruggable.” Therefore, there remains a need for the development and characterization of molecules that inhibit the interactions of protein targets.